Alpha-1-Antitrypsin

(All numbering and residues are taken from first PDB file)

Bending Residue Dihedral Analysis

Residue i Residue i+1 Distance of hinge axis to residue i in conformer 1 (A) Distance of hinge axis to residue i in conformer 2 (A) Change in psi (i) (deg) Change in phi (i+1) (deg) Angle of psi(i) axis to hinge axis conformer 1 (deg) Angle of psi(i) axis to hinge axis conformer 2 (deg) Percentage Progress  LYS-342   LYS-343  32.5 33.1 -24.8 -23.6 82.4 103.7 1.2  LYS-343   GLY-344  35.2 35.5 -178.1 -30.9 143.1 136.6 93.9  GLY-344   CYS-345  38.3 34.0 1.3 -38.6 108.2 88.6 9.1  CYS-345   GLU-346  42.1 31.5 -32.4 -37.3 69.6 65.8 23.1  LEU-353   GLU-354  48.3 31.0 -61.1 72.1 146.2 58.3 7.0  GLU-354   ALA-355  46.8 31.7 -8.8 -9.8 96.7 131.4 -22.2  ALA-355   ILE-356  47.7 34.2 5.8 -29.4 56.4 128.5 -10.6  ILE-356   PRO-357  45.3 35.6 36.8 18.6 55.3 48.1 54.6  PRO-357   ARG-358  46.0 38.0 -53.3 21.6 71.0 134.0 -24.8  ARG-358   SER-359  46.7 37.0 166.0 -59.0 73.4 96.9 58.8  SER-359   ILE-360  43.7 37.9 -41.2 24.8 49.0 159.2 8.5  ILE-360   PRO-361  40.6 38.8 -166.9 30.8 101.2 95.8 27.2  PRO-361   PRO-362  38.0 38.4 -26.9 25.9 89.4 99.5 11.4 Graph shows rotational transition at bending residues and can be used to identify hinge bending residues. Probably only informative for interdomain rotations greater than 20 degrees